The general aim of this SCORE application is the upgrade of physical and human resources at the University of Puerto Rico at Humacao (UPRH) in order to increase and improve its biomedical research activity. The following goals are set in pursuing these major aims: (1) to increase the biomedical research capacity at UPRH;(2) to increase the number of natural sciences faculty at UPRH involved in biomedical research and the number of biomedical research collaborations with research-intensive institutions;(3) to increase the number of biomedical research collaborations with research-intensive institutions;(4) to increase the number of submitted biomedical research grant applications from UPRH to non-MBRS extramural biomedical research agencies;and (5) to increase the biomedical research productivity at UPRH. Goal 1 will be achieved by hiring a full-time technician for the operation and maintenance of our most sophisticated MBRS-funded equipment. Goal 2 will be accomplished starting with the addition of an electrochemist to our SCORE project. This investigator is submitting a biomedical research proposal in this application dealing with developing a new system for membrane protein crystallization, using the self-assembled monolayers methods (SAMs). Five other research investigators from the Chemistry department are also submitting research proposals in this application. One of these Chemistry projects deals with a study of the solvent dependence of enzyme enantioselectivity with the purpose of understanding and improving enzyme's activity, stability and enantioselectivity in organic solvents for the small and large scale synthesis of bio-relevant compounds. A second project looks for the developing of new phenothiazine derivatives (neurologically active compounds) with less undesirable photocytotoxic effects, as well as understanding the mechanisms these photocytotoxic effects. A third project proposes the design of improved methods for the estereoselective preparation of diverse kind of amines with potential neurological effects. A fourth Chemistry project deals with a systematic study of different [unreadable]-hairpin structures in proteins using isotopic labeling along the primary amino acid sequence to understand protein folding dynamics. A fifth Chemistry subproject will study quinone roles in NO reduction and production enhancements and tumor-targeted toxicity of alkylating quinones. It is expected that the development of these projects will improve the possibilities of producing more research proposal applications to other extramural agencies, more research collaborations and an increase in peer-reviewed publications with the concomitant recognition of our faculty and students in the international biomedical research community.